##gff-version 3 Q91YM2 UniProtKB Chain 1 1499 . . . ID=PRO_0000056731;Note=Rho GTPase-activating protein 35 Q91YM2 UniProtKB Domain 270 327 . . . Note=FF 1 Q91YM2 UniProtKB Domain 368 422 . . . Note=FF 2 Q91YM2 UniProtKB Domain 429 483 . . . Note=FF 3 Q91YM2 UniProtKB Domain 485 550 . . . Note=FF 4 Q91YM2 UniProtKB Domain 592 767 . . . Note=PG1 pseudoGTPase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01199 Q91YM2 UniProtKB Domain 783 947 . . . Note=PG2 pseudoGTPase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01200 Q91YM2 UniProtKB Domain 1249 1436 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 Q91YM2 UniProtKB Region 1 266 . . . Note=Has GTPase activity%2C required for proper localization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11044403;Dbxref=PMID:11044403 Q91YM2 UniProtKB Region 1124 1148 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q91YM2 UniProtKB Region 1177 1207 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q91YM2 UniProtKB Region 1213 1236 . . . Note=Required for phospholipid binding and regulation of the substrate preference;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Region 1446 1499 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q91YM2 UniProtKB Compositional bias 1124 1139 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q91YM2 UniProtKB Compositional bias 1182 1196 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q91YM2 UniProtKB Compositional bias 1470 1485 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q91YM2 UniProtKB Binding site 28 28 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Binding site 33 37 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Binding site 52 52 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Binding site 56 56 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Binding site 95 97 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Binding site 201 203 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Binding site 229 231 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 308 308 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 589 589 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 770 770 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 773 773 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 970 970 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 975 975 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 985 985 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 1072 1072 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 1087 1087 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 1105 1105 . . . Note=Phosphotyrosine%3B by ABL2 and PTK6;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16971514,ECO:0007744|PubMed:17947660,ECO:0007744|PubMed:18034455,ECO:0007744|PubMed:21183079;Dbxref=PMID:16971514,PMID:17947660,PMID:18034455,PMID:21183079 Q91YM2 UniProtKB Modified residue 1134 1134 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 1142 1142 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 1150 1150 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 1176 1176 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 1179 1179 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q91YM2 UniProtKB Modified residue 1221 1221 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 1226 1226 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 1236 1236 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NRY4 Q91YM2 UniProtKB Modified residue 1472 1472 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760 Q91YM2 UniProtKB Modified residue 1476 1476 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760 Q91YM2 UniProtKB Modified residue 1480 1480 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760 Q91YM2 UniProtKB Modified residue 1483 1483 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760 Q91YM2 UniProtKB Mutagenesis 1396 1396 . . . Note=In ENU mutant Arhgap35-D34%3B mutant animals show hypodysplastic kidneys and neural tube closure defects%3B the number of ciliated cells and cilia average length are drastically reduced in the proximal tubules. Results in loss of activation of GTP hydrolysis. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26859289;Dbxref=PMID:26859289 Q91YM2 UniProtKB Mutagenesis 1472 1472 . . . Note=Reduces phosphorylation by GSK3B by 50%25. No effect on polarized cell migration. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760 Q91YM2 UniProtKB Mutagenesis 1476 1476 . . . Note=Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. Affects polarized cell migration. Increases RhoGAP catalytic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760 Q91YM2 UniProtKB Mutagenesis 1480 1480 . . . Note=Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. Affects polarized cell migration. Increases RhoGAP catalytic activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760 Q91YM2 UniProtKB Mutagenesis 1483 1483 . . . Note=Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. No effect on polarized cell migration. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18502760;Dbxref=PMID:18502760